(R)-3-(benzyl((R)-1-phenylethyl)amino)-2-methylpropan-1-ol | 1400685-01-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (R)-3-(benzyl((R)-1-phenylethyl)amino)-2-methylpropan-1-ol
• CAS: 1400685-01-9
• 化学式: C₁₉H₂₅NO
• 分子量: 283.414
• InChiKey: BQCLVPDWUMOGGS-IAGOWNOFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.88
• 重原子数：
  21.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  23.47
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  (R)-3-(benzyl((R)-1-phenylethyl)amino)-2-methylpropan-1-ol 在 palladium 10% on activated carbon 、 甲酸铵 作用下， 以 叔丁醇 为溶剂， 生成 (R)-3-amino-2-methyl-1-propanol
  参考文献：
  名称：

  Design Strategies for the Sequence-Based Mimicry of Side-Chain Display in Protein β-Sheets by α/β-Peptides

  摘要：

  The sophistication of folding patterns and functions displayed by unnatural-backbone oligomers has increased tremendously in recent years. Design strategies for the mimicry of tertiary structures seem within reach; however, a general method for the mimicry of sheet segments in the context of a folded protein is an unmet need preventing realization of this goal. Previous work has shown that 1 -> 1 alpha ->beta-residue substitutions at cross-strand positions in a hairpin-forming alpha-peptide sequence can generate an alpha/beta-peptide analogue that folds in aqueous conditions but with a change in side-chain display relative to the natural sequence; this change would prevent application of single beta-residue substitutions in a larger protein. Here, we evaluate four different substitution strategies based on replacement of alpha alpha dipeptide segments for the ability to retain both sheet folding encoded by a parent alpha-peptide sequence as well as nativelike side-chain display in the vicinity of the beta-residue insertion point. High-resolution structure determination and thermodynamic analysis of folding by multidimensional NMR suggest that three of the four designs examined are applicable to larger proteins.

  DOI：

  10.1021/ja306311r
• 作为产物：
  描述：

  (R)-N-benzyl-N-(methoxymethyl)-1-phenylethan-1-amine 、 丙醛 在 D-脯氨酸 、 sodium tetrahydroborate 作用下， 以 N,N-二甲基甲酰胺 、 甲醇 为溶剂， 反应 24.75h， 以43%的产率得到(R)-3-(benzyl((R)-1-phenylethyl)amino)-2-methylpropan-1-ol
  参考文献：
  名称：

  Design Strategies for the Sequence-Based Mimicry of Side-Chain Display in Protein β-Sheets by α/β-Peptides

  摘要：

  The sophistication of folding patterns and functions displayed by unnatural-backbone oligomers has increased tremendously in recent years. Design strategies for the mimicry of tertiary structures seem within reach; however, a general method for the mimicry of sheet segments in the context of a folded protein is an unmet need preventing realization of this goal. Previous work has shown that 1 -> 1 alpha ->beta-residue substitutions at cross-strand positions in a hairpin-forming alpha-peptide sequence can generate an alpha/beta-peptide analogue that folds in aqueous conditions but with a change in side-chain display relative to the natural sequence; this change would prevent application of single beta-residue substitutions in a larger protein. Here, we evaluate four different substitution strategies based on replacement of alpha alpha dipeptide segments for the ability to retain both sheet folding encoded by a parent alpha-peptide sequence as well as nativelike side-chain display in the vicinity of the beta-residue insertion point. High-resolution structure determination and thermodynamic analysis of folding by multidimensional NMR suggest that three of the four designs examined are applicable to larger proteins.

  DOI：

  10.1021/ja306311r